Factors resisting protein adsorption on hydrophilic/hydrophobic self-assembled monolayers terminated with hydrophilic hydroxyl groups

doi:10.1088/1674-1056/ad39ca

中国物理B ›› 2024, Vol. 33 ›› Issue (6): 68701-068701.doi: 10.1088/1674-1056/ad39ca

Factors resisting protein adsorption on hydrophilic/hydrophobic self-assembled monolayers terminated with hydrophilic hydroxyl groups

Dangxin Mao(毛党新), Yuan-Yan Wu(吴园燕)†, and Yusong Tu(涂育松)‡

College of Physics Science and Technology, Yangzhou University, Yangzhou 225009, China

收稿日期:2024-02-21 修回日期:2024-03-16 接受日期:2024-04-03 出版日期:2024-06-18 发布日期:2024-06-18
通讯作者: Yuan-Yan Wu, Yusong Tu E-mail:yywu@yzu.edu.cn;ystu@yzu.edu.cn
基金资助:
Project supported by the National Natural Science Foundation of China (Grants No. 12075201), the Science and Technology Planning Project of Jiangsu Province, China (Grant No. BK20201428), the Postgraduate Research & Practice Innovation Program of Jiangsu Province, China (Grant No. KYCX21 3193), and the Special Program for Applied Research on Supercomputation of the NSFC-Guangdong Joint Fund (the second phase).

Factors resisting protein adsorption on hydrophilic/hydrophobic self-assembled monolayers terminated with hydrophilic hydroxyl groups

Dangxin Mao(毛党新), Yuan-Yan Wu(吴园燕)†, and Yusong Tu(涂育松)‡

College of Physics Science and Technology, Yangzhou University, Yangzhou 225009, China

Received:2024-02-21 Revised:2024-03-16 Accepted:2024-04-03 Online:2024-06-18 Published:2024-06-18
Contact: Yuan-Yan Wu, Yusong Tu E-mail:yywu@yzu.edu.cn;ystu@yzu.edu.cn
Supported by:
Project supported by the National Natural Science Foundation of China (Grants No. 12075201), the Science and Technology Planning Project of Jiangsu Province, China (Grant No. BK20201428), the Postgraduate Research & Practice Innovation Program of Jiangsu Province, China (Grant No. KYCX21 3193), and the Special Program for Applied Research on Supercomputation of the NSFC-Guangdong Joint Fund (the second phase).

1. 2024-068701-SI.pdf(1175KB)

摘要/Abstract

摘要： The hydroxyl-terminated self-assembled monolayer (OH-SAM), as a surface resistant to protein adsorption, exhibits substantial potential in applications such as ship navigation and medical implants, and the appropriate strategies for designing anti-fouling surfaces are crucial. Here, we employ molecular dynamics simulations and alchemical free energy calculations to systematically analyze the factors influencing resistance to protein adsorption on the SAMs terminated with single or double OH groups at three packing densities ($\varSigma = 2.0 $nm$^{-2}$, 4.5nm$^{-2}$, and 6.5nm$^{-2}$), respectively. For the first time, we observed that the compactness and order of interfacial water enhance its physical barrier effect, subsequently enhancing the resistance of SAM to protein adsorption. Notably, the spatial hindrance effect of SAM leads to the embedding of protein into SAM, resulting in a lack of resistance of SAM towards protein. Furthermore, the number of hydroxyl groups per unit area of double OH-terminated SAM at $\varSigma = 6.5 $nm$^{-2}$ is approximately 2 to 3 times that of single OH-terminated SAM at $\varSigma = 6.5 $nm$^{-2}$ and 4.5nm$^{-2}$, consequently yielding a weaker resistance of double OH-terminated SAM towards protein. Meanwhile, due to the structure of SAM itself, i.e., the formation of a nearly perfect ice-like hydrogen bond structure, the SAM exhibits the weakest resistance towards protein. This study will complement and improve the mechanism of OH-SAM resistance to protein adsorption, especially the traditional barrier effect of interfacial water.

关键词: molecular dynamics simulation, self-assembled monolayer, resistance to protein adsorption, hydrogen bond, interfacial water

Abstract: The hydroxyl-terminated self-assembled monolayer (OH-SAM), as a surface resistant to protein adsorption, exhibits substantial potential in applications such as ship navigation and medical implants, and the appropriate strategies for designing anti-fouling surfaces are crucial. Here, we employ molecular dynamics simulations and alchemical free energy calculations to systematically analyze the factors influencing resistance to protein adsorption on the SAMs terminated with single or double OH groups at three packing densities ($\varSigma = 2.0 $nm$^{-2}$, 4.5nm$^{-2}$, and 6.5nm$^{-2}$), respectively. For the first time, we observed that the compactness and order of interfacial water enhance its physical barrier effect, subsequently enhancing the resistance of SAM to protein adsorption. Notably, the spatial hindrance effect of SAM leads to the embedding of protein into SAM, resulting in a lack of resistance of SAM towards protein. Furthermore, the number of hydroxyl groups per unit area of double OH-terminated SAM at $\varSigma = 6.5 $nm$^{-2}$ is approximately 2 to 3 times that of single OH-terminated SAM at $\varSigma = 6.5 $nm$^{-2}$ and 4.5nm$^{-2}$, consequently yielding a weaker resistance of double OH-terminated SAM towards protein. Meanwhile, due to the structure of SAM itself, i.e., the formation of a nearly perfect ice-like hydrogen bond structure, the SAM exhibits the weakest resistance towards protein. This study will complement and improve the mechanism of OH-SAM resistance to protein adsorption, especially the traditional barrier effect of interfacial water.

Key words: molecular dynamics simulation, self-assembled monolayer, resistance to protein adsorption, hydrogen bond, interfacial water

中图分类号: (Molecular dynamics simulation)

87.10.Tf

64.75.Yz (Self-assembly) 87.15.K- (Molecular interactions; membrane-protein interactions) 68.08.-p (Liquid-solid interfaces)

Dangxin Mao(毛党新), Yuan-Yan Wu(吴园燕), and Yusong Tu(涂育松). Factors resisting protein adsorption on hydrophilic/hydrophobic self-assembled monolayers terminated with hydrophilic hydroxyl groups[J]. 中国物理B, 2024, 33(6): 68701-068701.

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Factors resisting protein adsorption on hydrophilic/hydrophobic self-assembled monolayers terminated with hydrophilic hydroxyl groups

Factors resisting protein adsorption on hydrophilic/hydrophobic self-assembled monolayers terminated with hydrophilic hydroxyl groups

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